2XK0

Solution structure of the Tudor domain from Drosophila Polycomblike (Pcl)

Summary for 2XK0

• Entry DOI: 10.2210/pdb2xk0/pdb
• NMR Information: BMRB: 17050
• Descriptor: POLYCOMB PROTEIN PCL (1 entity in total)
• Functional Keywords: transcription, aromatic cage
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Total number of polymer chains: 1
• Total formula weight: 7588.44

Authors

Friberg, A.,Oddone, A.,Klymenko, T.,Mueller, J.,Sattler, M. (deposition date: 2010-07-07, release date: 2010-08-11, Last modification date: 2024-06-19)

Primary citation

Friberg, A.,Oddone, A.,Klymenko, T.,Mueller, J.,Sattler, M.
Structure of an Atypical Tudor Domain in the Drosophila Polycomblike Protein
Protein Sci., 19:1906-, 2010

PubMed Abstract: Post-translational modifications of histone tails are among the most prominent epigenetic marks and play a critical role in transcriptional control at the level of chromatin. The Polycomblike (Pcl) protein is part of a histone methyltransferase complex (Pcl-PRC2) responsible for high levels of histone H3 K27 trimethylation. Studies in Drosophila larvae suggest that Pcl is required for anchoring Pcl-PRC2 at target genes, but how this is achieved is unknown. Pcl comprises a Tudor domain and two PHD fingers. These domains are known to recognize methylated lysine or arginine residues and could contribute to targeting of Pcl-PRC2. Here, we report an NMR structure of the Tudor domain from Drosophila Pcl (Pcl-Tudor) and binding studies with putative ligands. Pcl-Tudor contains an atypical, incomplete aromatic cage that does not interact with known Tudor domain ligands, such as methylated lysines or arginines. Interestingly, human Pcl orthologs exhibit a complete aromatic cage, suggesting that they may recognize methylated lysines. Structural comparison with other Tudor domains suggests that Pcl-Tudor may engage in intra- or intermolecular interactions through an exposed hydrophobic surface patch.

PubMed: 20669242
DOI: 10.1002/PRO.476

Experimental method

SOLUTION NMR